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130 results about "Alpha helix" patented technology

The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located three or four residues earlier along the protein sequence.

Dideoxynucleotide-triphosphate utilization by the hyper-thermophilic DNA polymerase from the archaeon Pyrococcus furiosus

Polymerases from the Pol I family which are able to efficiently use ddNTPs have demonstrated a much improved performance when used to sequence DNA. A number of mutations have been made to the gene coding for the Pol II family DNA polymerase from the archaeon Pyrococcus furiosus with the aim of improving ddNTP utilisation. "Rational" alterations to amino acids likely to be near the dNTP binding site (based on sequence homologies and structural information) did not yield the desired level of selectivity for ddNTPs. However, alteration at four positions (Q472, A486, L490 and Y497) gave rise to variants which incorporated ddNTPs better than the wild type, allowing sequencing reactions to be carried out at lowered ddNTP:dNTP ratios. Wild type Pfu-Pol required a ddNTP:dNTP ratio of 30:1; values of 5:1 (Q472H), 1:3 (L490Y), 1:5 (A486Y) and 5:1 (Y497A) were found with the four mutants; A486Y representing a 150-fold improvement over the wild type. A486, L490 and Y407 are on an alpha-helix that lines the dNTP binding groove, but the side chains of the three amino acids point away from this groove; Q472 is in a loop that connects this alpha-helix to a second long helix. None of the four amino acids can contact the dNTP directly. Therefore, the increased selectivity for ddNTPs is likely to arise from two factors: 1) Small overall changes in conformation that subtly alter the nucleotide triphosphate binding site such that ddNTPs become favoured; 2) interference with a conformational change that may be critical both for the polymerisation step and discrimination between different nucleotide triphosphates.
Owner:GE HEALTHCARE BIO SCI CORP

Efficient alpha-helix antibacterial peptide GV and preparation method and application thereof

The invention relates to an efficient alpha-helix antibacterial peptide GV and a preparation method and application thereof. The antibacterial peptide GV is an antibacterial peptide with high cell selectivity and achieves an optimal point of junction of the antibacterial activity and cell toxicity of the antibacterial peptide. A sequence of the antibacterial peptide GV is represented by a sequence table SEQ ID No. 1. The preparation method comprises the following steps: (1) carrying out designing in accordance with alpha-helix peptide GRX2RX3RX2RG serves as a template, so as to obtain a brand-new antibacterial peptide GV, wherein X= V; (2) synthesizing a polypeptide crude product through a polypeptide synthesizer by a solid-phase chemical synthesis method; purifying the synthesized polypeptide by using out-phase high-performance liquid chromatography, and carrying out identification on the synthesized polypeptide by using electrospray mass spectrography, thereby preparing the polypeptide. The antibacterial peptide GV provided by the invention has relatively high bacteriostatic activity and relatively low hemolytic activity and is the highest in therapeutic index, thereby having great development potential.
Owner:NORTHEAST AGRICULTURAL UNIVERSITY

Polypeptide, lipoprotein-like nano particle and application thereof

The invention discloses a polypeptide, a lipoprotein-like nano particle (LNP) and application thereof. The LNP contains at least one phospholipid and at least one polypeptide. A polypeptide series helix-ring-helix structure polypeptide contains at least two amphiphilic alpha helixes, and the two amphiphilic alpha helixes are connected through at least one connecting peptide containing a cyclic structure. The helix part of the polypeptide is imbedded into a lipoprotein-like nano particle surface layer, stable formation of lipid nano particles with uniform size and relatively small particle diameters can be promoted, meanwhile cyclic sequences stretch out of the surfaces of the lipoprotein-like nano particles, and functional sequence insertion is further facilitated, so that multi-functionalization of the LNP is realized. Moreover, the application of the LNP can be further expanded by using an LNP packaged lyophobically functional substance, and for example, the LNP can be used as a drug delivery system; the drug delivery system has the characteristics of being low in toxicity and high in stability, facilitating functionalization and the like, and a simple, convenient and effective means is provided for target killing of cancer cells and cell and tissue imaging.
Owner:SUZHOU INST OF NANO TECH & NANO BIONICS CHINESE ACEDEMY OF SCI
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